Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A functional map of the human intrinsically disordered proteome.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Conformational Ensembles of the Disordered 4E-BP2:eIF4E Complex Restrained by smFRET Experiments.

bioRxiv : the preprint server for biology·2026
Same author

BRD4 recruitment desilences transcription without erasure or depletion of repressive chromatin.

bioRxiv : the preprint server for biology·2026
Same author

IDPForge: Deep Learning of Proteins with Global and Local Regions of Disorder.

bioRxiv : the preprint server for biology·2026
Same author

PRRC2A, PRRC2B and PRRC2C are Stress Granule Proteins that Promote Translation Through Association with the eIF3 complex.

bioRxiv : the preprint server for biology·2026
Same author

Density transitions in the regulation of transcription.

Molecular cell·2026

Related Experiment Video

Updated: May 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.

Julie D Forman-Kay1, Tanja Mittag

  • 1Molecular Structure and Function, Hospital for Sick Children, Toronto, ON, M5G 1X8, Canada; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.

Structure (London, England : 1993)
|September 10, 2013
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) lack stable structures, posing challenges for traditional methods. Recent advancements are unifying the understanding of protein dynamics, disorder, and function.

More Related Videos

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET
05:13

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET

Published on: January 12, 2024

Related Experiment Videos

Last Updated: May 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET
05:13

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET

Published on: January 12, 2024

Area of Science:

  • Structural Biology
  • Biochemistry
  • Protein Science

Background:

  • Intrinsically disordered proteins (IDPs) present unique challenges to structural biology due to their lack of persistent structure.
  • Standard characterization methods for folded proteins are often inapplicable to IDPs.
  • IDPs deviate from the traditional structure/function paradigm but are increasingly recognized for their biological importance.

Purpose of the Study:

  • To provide a historical perspective on the investigation of IDPs.
  • To summarize the sequence features and physical forces underlying IDP properties.
  • To contribute to a unified understanding of structure-dynamics-disorder/function relationships.

Main Methods:

  • Review of historical investigations into IDPs.
  • Analysis of sequence features contributing to protein disorder.
  • Examination of physical forces governing IDP behavior.

Main Results:

  • IDPs, despite lacking stable structures, are crucial for various biological functions.
  • A continuum of protein states exists, linking conformational energetics, dynamics, and compactness.
  • The interplay between folded and disordered regions influences protein function.

Conclusions:

  • The study of IDPs has evolved significantly, necessitating new tools and approaches.
  • Understanding IDPs requires considering a spectrum of conformational states and dynamics.
  • Sequence features and physical forces are key determinants of IDP structural, functional, and evolutionary properties.